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	Structure of protein O-mannose kinase reveals a unique active site architecture; Structure of protein O-mannose kinase reveals a unique active site architecture
	Qinyu Zhu ; Qiuyu Fu ; Wei Wang ; Xing Chen ; Niu Huang ; Liping Yu ; Junyu Xiao
	2016
关键词	mannose elusive laminin glycan fluoride biosynthesis underlying moiety residues providing mannose elusive laminin glycan fluoride biosynthesis underlying moiety residues providing
英文摘要	The"pseudokinase"Sg K196 is a protein O-mannose kinase(POMK)that catalyzes an essential phosphorylation step during biosynthesis of the laminin-binding glycan ona-dystroglycan.However,the catalytic mechanism underlying this activity remains elusive.Here we present the crystal structure of Danio rerio POMK in complex with Mg~(2+) ions,ADP,aluminum fluoride,and; The"pseudokinase"Sg K196 is a protein O-mannose kinase(POMK)that catalyzes an essential phosphorylation step during biosynthesis of the laminin-binding glycan ona-dystroglycan.However,the catalytic mechanism underlying this activity remains elusive.Here we present the crystal structure of Danio rerio POMK in complex with Mg~(2+) ions,ADP,aluminum fluoride,and; 中国晶体学会; 1
语种	英语
出处	中国晶体学会第六届学术年会暨会员代表大会（大分子晶体学分会）
内容类型	其他
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/479690]
专题	化学与分子工程学院 生命科学学院
推荐引用方式 GB/T 7714	Qinyu Zhu,Qiuyu Fu,Wei Wang,et al. Structure of protein O-mannose kinase reveals a unique active site architecture, Structure of protein O-mannose kinase reveals a unique active site architecture. 2016-01-01.

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